Research workbench
Crystal structure of mltf from pseudomonas aeruginosa in the presence of tetrasaccharide and tetrapeptide
Analyse Crystal structure of mltf from pseudomonas aeruginosa in the presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AA3
- Type
- protein
- Length
- 5,002 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane-bound lytic murein transglycosylase F
- UniProt
- Q9HXN1
- Ligands
- GLU
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 8 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, K | Membrane-bound lytic murein transglycosylase F | protein | 417 | 48% helix, 17% strand | Q9HXN1 |
| B | Membrane-bound lytic murein transglycosylase F | protein | 417 | 48% helix, 18% strand | Q9HXN1 |
| C | Membrane-bound lytic murein transglycosylase F | protein | 418 | 48% helix, 16% strand | Q9HXN1 |
| D, H | Membrane-bound lytic murein transglycosylase F | protein | 415 | 48% helix, 17% strand | Q9HXN1 |
| E | Membrane-bound lytic murein transglycosylase F | protein | 418 | 48% helix, 17% strand | Q9HXN1 |
| F, G, J | Membrane-bound lytic murein transglycosylase F | protein | 416 | 48% helix, 18% strand | Q9HXN1 |
| I | Membrane-bound lytic murein transglycosylase F | protein | 418 | 48% helix, 17% strand | Q9HXN1 |
| L | Membrane-bound lytic murein transglycosylase F | protein | 419 | 48% helix, 16% strand | Q9HXN1 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 530 | 0.80 | 0.86 | 53 | empty |
| 2 | 959 | 0.80 | 0.81 | 69 | empty |
| 3 | 550 | 0.80 | 0.86 | 52 | empty |
| 4 | 882 | 0.79 | 0.82 | 65 | empty |
| 5 | 519 | 0.79 | 0.86 | 48 | empty |
Interfaces
15 interfaces between chains.
- H–L · 876 Ų buried · 9 hydrogen bonds · protein-protein
- A–F · 829 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 822 Ų buried · 10 hydrogen bonds · protein-protein
- C–H · 646 Ų buried · 2 hydrogen bonds · protein-protein
- B–F · 395 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- Q9HXN1 · AlphaFold monomer V2.0 prediction for membrane-bound lytic murein transglycosylase F… · a predicted model of the same protein · chain D against A, TM-score 0.66
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9HXN1
- Elsewhere: RCSB PDB 5AA3 · PDBe 5AA3 · UniProt Q9HXN1
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